ID   Y780_STAAR              Reviewed;         305 AA.
AC   Q6GIR5;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Putative lipid kinase SAR0780;
DE            EC=2.7.1.-;
GN   OrderedLocusNames=SAR0780;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
RN   [2]
RP   LACK OF FUNCTION AS A DIACYLGLYCEROL KINASE.
RX   PubMed=17535816; DOI=10.1074/jbc.m703536200;
RA   Jerga A., Lu Y.-J., Schujman G.E., de Mendoza D., Rock C.O.;
RT   "Identification of a soluble diacylglycerol kinase required for
RT   lipoteichoic acid production in Bacillus subtilis.";
RL   J. Biol. Chem. 282:21738-21745(2007).
CC   -!- FUNCTION: May catalyze the ATP-dependent phosphorylation of lipids
CC       other than diacylglycerol (DAG). In fact, is not able to exhibit
CC       diacylglycerol kinase activity in vitro.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. This ion appears to have a
CC       structural role and is required for catalytic activity. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the diacylglycerol/lipid kinase family.
CC       {ECO:0000305}.
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DR   EMBL; BX571856; CAG39790.1; -; Genomic_DNA.
DR   RefSeq; WP_000429002.1; NC_002952.2.
DR   AlphaFoldDB; Q6GIR5; -.
DR   SMR; Q6GIR5; -.
DR   KEGG; sar:SAR0780; -.
DR   HOGENOM; CLU_045532_1_0_9; -.
DR   OMA; LPGGTCN; -.
DR   OrthoDB; 869726at2; -.
DR   Proteomes; UP000000596; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.10330; -; 1.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
DR   InterPro; IPR005218; Diacylglycerol/lipid_kinase.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   InterPro; IPR045540; YegS/DAGK_C.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   Pfam; PF19279; YegS_C; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SUPFAM; SSF111331; SSF111331; 1.
DR   TIGRFAMs; TIGR00147; TIGR00147; 1.
DR   PROSITE; PS50146; DAGK; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Lipid biosynthesis; Lipid metabolism; Magnesium;
KW   Metal-binding; Nucleotide-binding; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Transferase.
FT   CHAIN           1..305
FT                   /note="Putative lipid kinase SAR0780"
FT                   /id="PRO_0000386504"
FT   DOMAIN          3..139
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   ACT_SITE        281
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   BINDING         74..80
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   BINDING         101
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT   BINDING         220
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         225
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   305 AA;  33613 MW;  89F955FDE99B8803 CRC64;
     MENKYTHGVL FYHEHSGLKN INQGIGEVTT ALSSICKHLS IQLSENEGDI IKYCQEIKAK
     DYAKDVDILF ILGGDGTVNE LINGVMTHDL QLPIGILPGG TFNDFTKTLN IAPNHKQASE
     QMISAQVGTY DVIKINNQYA LNFVGLGLIV QNAENVQDGS KDIFGKLSYI GSTVKTLLNP
     TQFNYQLSID DKTYSGETTM ILSANGPFIG GSRIPLTDLS PQDGELNTFI FNEQSFSILN
     DIFKKRDSMN WNEITQGIEH IPGKKISLTT DPTMKVDIDG EISLETPIDI EVIPNAIQLL
     TVNDL